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The natural history of MCRPE is in relation to the role of MAPKAPK3 in BM modeling, vascular endothelial growth factor activity, retinal pigment epithelial responses
A dominant mutation in MAPKAPK3 causes a new retinal dystrophy involving Bruch's membrane and retinal pigment epithelium.
MK3 modulation affects BMI1-dependent and independent cell cycle check-points
findings reveal MK2/MK3 as crucial stress-responsive kinases that promote autophagy through Beclin 1 S90 phosphorylation
Hepatitis C virus core protein interacted with MAPKAPK3 through amino acid residues 41 to 75 of core and the N-terminal half of kinase domain of MAPKAPK3.
Identified CREB activators MAPKAPK3 and FHL5 as mediators of intimal hyperplasia in vein graft samples.
A high-resolution (1.9 A) crystal structure of the highly homologous MK3 in complex with a pharmaceutical lead compound is presented.
In the preconditioned heart, genes for MAPKAP kinase 3 were up-regulated.
3pK is transported to the cytoplasm upon both stress and mitogenic stimulation. While kinetics of nuclear export are similar in both situations, the activation pattern differs substantially.
this study shows that the loss of MK3 in mast cells decreases the IL-33-induced leukocyte recruitment and the resulting skin inflammation
MK2/3 cascade plays a strategic role in controlling synaptic plasticity and cognition.
This study showed that cmpd28, a Mapkapk2/3 inhibitor, represents a potentially new approach to type 2 diabetes therapy.
Mk3-/- mice, challenged with IAV infection, show a strong shift toward an innate NK cell and adaptive Th1 immune response and a resistance to influenza.
MAPKAPK-3 regulates SERCA2a expression and fiber type composition to modulate skeletal muscle and cardiomyocyte function.
Protein kinases MK2 and MK3 play critical roles in a mouse model of glomerulonephritis.
MK2 regulates LPS-induced IFNbeta expression and downstream STAT3 activation as it restrains MK3 from mediating negative regulatory effects
p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins.
Results suggest that both MK3.1 and MK3.2 are translated in the heart but differ in their subcellular localization.
The swine MAPKAPK3 gene might play an important role in the growth and development differences between mini-type Diannan small-ear pigs and large-type Diannan small-ear pigs.
This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation. Alternate splicing results in multiple transcript variants that encode the same protein.
MAP kinase-activated protein kinase 3
, MAPK-activated protein kinase 3
, MAPKAP kinase 3
, chromosome 3p kinase
, mitogen activated protein kinase-activated protein kinase 3
, mitogen-activated protein kinase-activated protein kinase 3
, MAP kinase-activated protein kinase 3-like